Arginine 357 of SecY is needed for SecA‐dependent initiation of preprotein translocation | Zendy

de Keyzer Jeanine | Zendy; Regeling Anouk | Zendy; Driessen Arnold J.M. | Zendy

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Arginine 357 of SecY is needed for SecA‐dependent initiation of preprotein translocation

Author(s) -

de Keyzer Jeanine,

Regeling Anouk,

Driessen Arnold J.M.

Publication year - 2007

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2007.03.081

Subject(s) - periplasmic space , translocon , chromosomal translocation , transmembrane protein , microbiology and biotechnology , transport protein , twin arginine translocation pathway , secretory protein , membrane transport protein , biology , biochemistry , membrane protein , transmembrane domain , atpase , chemistry , escherichia coli , biophysics , secretion , membrane , enzyme , gene , receptor

The Escherichia coli SecYEG complex forms a transmembrane channel for both protein export and membrane protein insertion. Secretory proteins and large periplasmic domains of membrane proteins require for translocation in addition the SecA ATPase. The conserved arginine 357 of SecY is essential for a yet unidentified step in the SecA catalytic cycle. To further dissect its role, we have analysed the requirement for R357 in membrane protein insertion. Although R357 substitutions abolish post‐translational translocation, they allow the translocation of periplasmic domains targeted co‐translationally by an N‐terminal transmembrane segment. We propose that R357 is essential for the initiation of SecA‐dependent translocation only.

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